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Structure of the leech protein saratin and characterization of its binding to collagen

Gronwald, Wolfram, Bomke, J., Maurer, T., Domogalla, B., Huber, F., Schumann, F., Kremer, W., Fink, F., Rysiok, T., Frech, M. and Kalbitzer, Hans Robert (2008) Structure of the leech protein saratin and characterization of its binding to collagen. J. Mol. Biol. 381 (4), pp. 913-927.

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Other URL: http://www.sciencedirect.com/science/article/pii/S0022283608007377


The leech protein Saratin from Hirudo medicinalis prevents thrombocyte aggregation by interfering with the first binding step of the thrombocytes to collagen by binding to collagen. We solved the three-dimensional structure of the leech protein Saratin in solution and identified its collagen binding site by NMR titration experiments. The NMR structure of Saratin consists of one α-helix and a ...


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Item type:Article
Date:September 2008
Institutions:Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner)
Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
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Keywords:Saratin structure; collagen interaction; leech protein; NMR; hemostasis
Dewey Decimal Classification:600 Technology > 610 Medical sciences Medicine
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Partially
Item ID:33610
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